Rose, R.J. and Verger, Denis and Daviter, Tina and Remaut, Han and Paci, E. and Waksman, Gabriel and Ashcroft, A.E. and Radford, S.E. (2008) Unraveling the molecular basis of subunit specificity in P pilus assembly by mass spectrometry. Proceedings of the National Academy of Sciences of the United States of America 105 (35), pp. 12873-12878. ISSN 0027-8424.Full text not available from this repository.
P pili are multisubunit fibers essential for the attachment of uropathogenic Escherichia coli to the kidney. These fibers are formed by the noncovalent assembly of six different homologous subunit types in an array that is strictly defined in terms of both the number and order of each subunit type. Assembly occurs through a mechanism termed “donor-strand exchange (DSE)” in which an N-terminal extension (Nte) of one subunit donates a β-strand to an adjacent subunit, completing its Ig fold. Despite structural determination of the different subunits, the mechanism determining specificity of subunit ordering in pilus assembly remained unclear. Here, we have used noncovalent mass spectrometry to monitor DSE between all 30 possible pairs of P pilus subunits and their Ntes. We demonstrate a striking correlation between the natural order of subunits in pili and their ability to undergo DSE in vitro. The results reveal insights into the molecular mechanism by which subunit ordering during the assembly of this complex is achieved.
|School or Research Centre:||Birkbeck Schools and Research Centres > School of Science > Biological Sciences|
|Date Deposited:||04 Aug 2010 14:09|
|Last Modified:||11 Oct 2016 15:26|
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